Full Text | PDF

Share on tweeters Share on facebook Share on linkedin Share on googleplus

Theranostics 2014; 4(7):701-707. doi:10.7150/thno.8803 This issue Cite

Short Research Communication

A New Method to Assay Protease Based on Amyloid Misfolding: Application to Prostate Cancer Diagnosis Using a Panel of Proteases Biomarkers

Hao Li1, Yue Huang1, Bin Zhang2, Dawei Yang1, Xiaoli Zhu2, Genxi Li1, 2✉

1. Department of Biochemistry and State Key Laboratory of Pharmaceutical Biotechnology, Nanjing University, Nanjing, China.
2. Laboratory of Biosensing Technology, School of Life Sciences, Shanghai University, Shanghai, China.

✉ Corresponding author: Department of Biochemistry and State Key Laboratory of Pharmaceutical Biotechnology, Nanjing University, Nanjing 210093, China. Fax: +86 25 83592510. E-mail address: genxiliedu.cn.

Citation:
Li H, Huang Y, Zhang B, Yang D, Zhu X, Li G. A New Method to Assay Protease Based on Amyloid Misfolding: Application to Prostate Cancer Diagnosis Using a Panel of Proteases Biomarkers. Theranostics 2014; 4(7):701-707. doi:10.7150/thno.8803. https://www.thno.org/v04p0701.htm
Other styles

File import instruction

Abstract

This paper reports a sensitive method with electrochemical technique to detect various proteases, which can be used for the diagnosis of prostate cancer. For the proposed assay method, the working electrode is modified with the peptide probes for the target proteases. These probes contain the substrate sequence of target proteases, as well as the seed peptide sequence that can accelerate the misfolding of amyloid-beta. If there are proteases in the test solution, after protease cleavage of the substrate peptides, the distal seed peptide will be removed from the electrode surface. So, in the absence of proteases, the seed peptides can initiate and accelerate amyloid-beta misfolding on the electrode surface. Consequently, the formed aggregates strongly block the electron transfer of the in-solution electroactive species with the electrode, resulting in suppressed signal readout. Nevertheless, in the presence of proteases, enzyme cleavage may lead to greatly mitigated protein misfolding and evident signal enhancement. Since the contrast in signal readout between the two cases can be amplified by using the protein misfolding step, high sensitivity suitable for direct detection of proteases in serum can be achieved. These results may suggest the feasibility of our new method for the detection of a panel of proteases in offering detailed diagnosis of prostate cancer and a better treatment of the cancer.

Keywords: prostate cancer, biomarker, protease, amyloid misfolding, electrochemical detection.

Citation styles

APA
Li, H., Huang, Y., Zhang, B., Yang, D., Zhu, X., Li, G. (2014). A New Method to Assay Protease Based on Amyloid Misfolding: Application to Prostate Cancer Diagnosis Using a Panel of Proteases Biomarkers. Theranostics, 4(7), 701-707. https://doi.org/10.7150/thno.8803.

ACS
Li, H.; Huang, Y.; Zhang, B.; Yang, D.; Zhu, X.; Li, G. A New Method to Assay Protease Based on Amyloid Misfolding: Application to Prostate Cancer Diagnosis Using a Panel of Proteases Biomarkers. Theranostics 2014, 4 (7), 701-707. DOI: 10.7150/thno.8803.

NLM
Li H, Huang Y, Zhang B, Yang D, Zhu X, Li G. A New Method to Assay Protease Based on Amyloid Misfolding: Application to Prostate Cancer Diagnosis Using a Panel of Proteases Biomarkers. Theranostics 2014; 4(7):701-707. doi:10.7150/thno.8803. https://www.thno.org/v04p0701.htm

CSE
Li H, Huang Y, Zhang B, Yang D, Zhu X, Li G. 2014. A New Method to Assay Protease Based on Amyloid Misfolding: Application to Prostate Cancer Diagnosis Using a Panel of Proteases Biomarkers. Theranostics. 4(7):701-707.

This is an open access article distributed under the terms of the Creative Commons Attribution (CC BY-NC) License. See http://ivyspring.com/terms for full terms and conditions.
Popup Image

©2024 Ivyspring International Publisher. Terms of use